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1J1G

Crystal structure of the RNase MC1 mutant N71S in complex with 5'-GMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0004519molecular_functionendonuclease activity
A0004521molecular_functionRNA endonuclease activity
A0005576cellular_componentextracellular region
A0006401biological_processRNA catabolic process
A0016829molecular_functionlyase activity
A0033897molecular_functionribonuclease T2 activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 5GP A 295
ChainResidue
AGLN9
AGLU84
ALYS87
AHIS88
AHOH310
AHOH388
AHIS34
ATRP37
ASER71
AVAL72
ALEU73
AARG74
APHE80
AHIS83

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 5GP A 296
ChainResidue
ASER63
AGLN64
ATHR67
AASN110
AALA122
APRO125
ALYS140
AHOH364
AHOH373
AHOH379

Functional Information from PROSITE/UniProt
site_idPS00530
Number of Residues8
DetailsRNASE_T2_1 Ribonuclease T2 family histidine active site 1. FtIHGLWP
ChainResidueDetails
APHE31-PRO38

site_idPS00531
Number of Residues12
DetailsRNASE_T2_2 Ribonuclease T2 family histidine active site 2. FwsHEWtKHGtC
ChainResidueDetails
APHE80-CYS91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10045, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H
ChainResidueDetails
AHIS34

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:10964705, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H
ChainResidueDetails
ATRP85

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10045, ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10446375, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H
ChainResidueDetails
AGLY89

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0000305|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCC, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H
ChainResidueDetails
AGLN9
AVAL72
AHIS88

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12731868, ECO:0000269|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H
ChainResidueDetails
AHIS34

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:12731868, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1V9H
ChainResidueDetails
AALA75

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15322360, ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H
ChainResidueDetails
ATRP81

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305|PubMed:10964705, ECO:0000305|PubMed:12731868, ECO:0000305|PubMed:15322360, ECO:0007744|PDB:1J1F, ECO:0007744|PDB:1J1G, ECO:0007744|PDB:1UCA, ECO:0007744|PDB:1UCD, ECO:0007744|PDB:1V9H
ChainResidueDetails
AGLU84

site_idSWS_FT_FI9
Number of Residues9
DetailsSITE: Involved in thermostability => ECO:0000269|PubMed:15322360
ChainResidueDetails
APHE102
ALYS103
AVAL106
AASN126
AARG128
ALYS145
AVAL163
AVAL166

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1bol
ChainResidueDetails
AHIS34
AGLU84
AHIS88

226707

PDB entries from 2024-10-30

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